000117177 001__ 117177
000117177 005__ 20240319081001.0
000117177 0247_ $$2doi$$a10.1016/j.jinorgbio.2022.111785
000117177 0248_ $$2sideral$$a128435
000117177 037__ $$aART-2022-128435
000117177 041__ $$aeng
000117177 100__ $$0(orcid)0000-0002-5431-2371$$aFamulari, Antonino$$uUniversidad de Zaragoza
000117177 245__ $$aEPR characterization of the heme domain of a self-sufficient cytochrome P450 (CYP116B5)
000117177 260__ $$c2022
000117177 5060_ $$aAccess copy available to the general public$$fUnrestricted
000117177 5203_ $$aCYP116B5 is a self-sufficient cytochrome P450 (CYP450) with interesting catalytic properties for synthetic purposes. When isolated, its heme domain can act as a peroxygenase on different substrates of biotechnological interest. Here, by means of continuous wave and advanced EPR techniques, the coordination environment of iron in the isolated CYP116B5 heme domain (CYP116b5hd) is characterized. The ligand-free protein shows the characteristic EPR spectrum of a low-spin (S = 1/2) FeIII-heme with gz = 2.440 ± 0.005, gy = 2.25 ± 0.01, gx = 1.92 ± 0.01]. These g-values reflect an electronic ground state very similar to classical P450 monooxygenases rather than P450 peroxygenases. Binding of imidazole results in g-values very close to the ones reported for CYP152 peroxygenases. The detection of hyperfine interactions through HYperfine Sub-level CORrElation (HYSCORE) Spectroscopy experiments, shows that this is due to a nitrogen-mediated axial coordination. This work adds a piece of experimental evidence to the research, aimed at elucidating the features that distinguish the classical P450 enzymes from peroxygenases. It shows that the electronic environment of heme iron of CYP116B5 in the resting state is similar to the classical P450 monooxygenases. Therefore, it is not the critical factor that confers to CYP116B5hd its peroxygenase-like activity, suggesting a crucial role of the protein matrix. © 2022 The Authors
000117177 536__ $$9info:eu-repo/grantAgreement/ES/DGA-FEDER/E35-20R$$9info:eu-repo/grantAgreement/EC/H2020/813209/EU/Paramagnetic Species in Catalysis Research. A Unified Approach Towards Heterogeneous, Homogeneous and Enzyme Catalysis/PARACAT$$9This project has received funding from the European Union’s Horizon 2020 research and innovation program under grant agreement No H2020 813209-PARACAT
000117177 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000117177 590__ $$a3.9$$b2022
000117177 592__ $$a0.646$$b2022
000117177 591__ $$aCHEMISTRY, INORGANIC & NUCLEAR$$b8 / 42 = 0.19$$c2022$$dQ1$$eT1
000117177 593__ $$aInorganic Chemistry$$c2022$$dQ1
000117177 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b126 / 285 = 0.442$$c2022$$dQ2$$eT2
000117177 593__ $$aBiochemistry$$c2022$$dQ2
000117177 594__ $$a7.0$$b2022
000117177 655_4 $$ainfo:eu-repo/semantics/conferenceObject$$vinfo:eu-repo/semantics/publishedVersion
000117177 700__ $$aCorreddu, Danilo
000117177 700__ $$aDi Nardo, Giovanna
000117177 700__ $$aGilardi, Gianfranco
000117177 700__ $$aChiesa, Mario
000117177 700__ $$0(orcid)0000-0002-1827-1250$$aGarcía-Rubio, Inés$$uUniversidad de Zaragoza
000117177 7102_ $$12003$$2395$$aUniversidad de Zaragoza$$bDpto. Física Materia Condensa.$$cÁrea Física Materia Condensada
000117177 773__ $$g231 (2022), 111785 [5 pp.]$$pJ. inorg. biochem.$$tJournal of Inorganic Biochemistry$$x0162-0134
000117177 8564_ $$s1147423$$uhttps://zaguan.unizar.es/record/117177/files/texto_completo.pdf$$yVersión publicada
000117177 8564_ $$s2607693$$uhttps://zaguan.unizar.es/record/117177/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000117177 909CO $$ooai:zaguan.unizar.es:117177$$particulos$$pdriver
000117177 951__ $$a2024-03-18-14:09:25
000117177 980__ $$aARTICLE